ArticleRapid communications in mass spectrometry : RCM2016
Targeted absolute quantitative proteomics with SILAC internal standards and unlabeled full-length protein calibrators (TAQSI).
Article in Rapid communications in mass spectrometry : RCM, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 25 citations in OpenAlex.
- Targeted Absolute Protein Quantification Using SILAC Internal Standard and Full-Length Protein Calibrators (TAQSI).Methods in molecular biology (Clifton, N.J.) · 2023Article
- Activity and Expression of Carboxylesterases and Arylacetamide Deacetylase in Human Ocular Tissues.Drug metabolism and disposition: the biological fate of chemicals · 2022Article
- Fungal secondary metabolites in food and pharmaceuticals in the era of multi-omics.Applied microbiology and biotechnology · 2022Review
- Plasma Carboxylesterase 1 Predicts Methylphenidate Exposure: A Proof-of-Concept Study Using Plasma Protein Biomarker for Hepatic Drug Metabolism.Clinical pharmacology and therapeutics · 2022Article
- Electromembrane Extraction and Mass Spectrometry for Liver Organoid Drug Metabolism Studies.Analytical chemistry · 2021Article
- Article
- Genome-wide pQTL analysis of protein expression regulatory networks in the human liver.BMC biology · 2020Article
- Carboxylesterase 1 and Precision Pharmacotherapy: Pharmacogenetics and Nongenetic Regulators.Drug metabolism and disposition: the biological fate of chemicals · 2020Review
- The effects of IFITM1 and IFITM3 gene deletion on IFNγ stimulated protein synthesis.Cellular signalling · 2019Article
- Label-free absolute protein quantification with data-independent acquisition.Journal of proteomics · 2019Article
- Mass Spectrometry-based Absolute Quantification of 20S Proteasome Status for ControlledMolecular & cellular proteomics : MCP · 2019Article
- Functional Study of Carboxylesterase 1 Protein Isoforms.Proteomics · 2019Article
- The Impact of Carboxylesterases in Drug Metabolism and Pharmacokinetics.Current drug metabolism · 2019Review
- A Comprehensive Functional Assessment of Carboxylesterase 1 Nonsynonymous Polymorphisms.Drug metabolism and disposition: the biological fate of chemicals · 2017Article
- Age-Dependent Absolute Abundance of Hepatic Carboxylesterases (CES1 and CES2) by LC-MS/MS Proteomics: Application to PBPK Modeling of Oseltamivir In Vivo Pharmacokinetics in Infants.Drug metabolism and disposition: the biological fate of chemicals · 2017Article
- Association of Oseltamivir Activation with Gender and Carboxylesterase 1 Genetic Polymorphisms.Basic & clinical pharmacology & toxicology · 2016Article
- Dabigatran etexilate activation is affected by the CES1 genetic polymorphism G143E (rs71647871) and gender.Biochemical pharmacology · 2016Article
- Revealing Higher Order Protein Structure Using Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2016Article
- Regulatory effects of genomic translocations at the human carboxylesterase-1 (CES1) gene locus.Pharmacogenetics and genomics · 2016Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
rationaleLiquid Chromatography/Mass Spectrometry (LC/MS)-based proteomics for absolute protein quantification has been increasingly utilized in both basic and clinical research. There is a great need to overcome some major hurdles of current absolute protein quantification methods, such as significant inter-assay variability and the high cost associated with the preparation of purified stable-isotope-labeled peptide/protein standards.
methodsWe developed a novel targeted absolute protein quantification method, named TAQSI, utilizing full-length isotope-labeled protein internal standards generated from SILAC (stable isotope labeling by amino acid in cell culture) and unlabeled full-length protein calibrators. This approach was applied to absolute quantification of carboxylesterase 1 (CES1), the primary human hepatic hydrolase, in a large set of human liver samples. Absolute CES1 quantities were derived from the standard calibration curves established from unlabeled CES1 protein calibrators and the isotope-labeled CES1 internal standards obtained from SILAC HepG2 cells.
resultsThe TAQSI assay was found to be accurate, precise, reproducible, and cost-effective. Importantly, protein quantification was not affected by various protein extraction and digestion protocols, and measurement errors associated with nonsynonymous variants can be readily identified and avoided. Furthermore, the TAQSI approach significantly simplifies the procedure of identifying the best performance surrogate peptides.
conclusionsThe TAQSI assay can be widely used for targeted absolute protein quantification in various biomedical research and clinical practice settings.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.